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Conserved domains on  [gi|338827709|ref|NP_001229770|]
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zinc finger protein 195 isoform 4 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development, and in regulating viral replication and transcription

CATH:  3.30.160.60
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 5.23e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 5.23e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338827709     8 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVGLTVCKPGLITCLEQRKEPWN 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-610 1.09e-07

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 206 FDNFSNLHRRNISNTGEKPFKC--QECGKSFQMLSFLTEHQKIHT-GKKFQKCGECGKTFIQCSHFTEPENIDTGEKPYK 282
Cdd:COG5048   43 FSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHnNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 283 CQECNNVIKTCSVLTKNriyaggehyrceefgkvFNQCSHLTEhehgteekpCKYEECSSVFISCSSLSNQQMILAGEKL 362
Cdd:COG5048  123 LSSHSLPPSSRDPQLPD-----------------LLSISNLRN---------NPLPGNNSSSVNTPQSNSLHPPLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 363 SKCETWYKGFNHSPNPSkhqrneIGGKPFKCEECDSIFKWFSDLTKHKRIHTGEKPYKCDECgkayTQSSHLSEHRRIHT 442
Cdd:COG5048  177 SKDPSSNLSLLISSNVS------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN----SQLSPKSLLSQSPS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 443 GEKP-YQCEECGKVFRTCSSLSNHKRTHSEE----------KPYTCEECGNIFKQLSDLTKHKKT--HTGE--KPYKCDE 507
Cdd:COG5048  247 SLSSsDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPY 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 508 --CGKNFTQSSNLIVHKRIHTGEKPYKCEECGR-------VFMWFSDITKHKKTHTGEKPYKCD--ECGKNFTQSSNLIV 576
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfsplLNNEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSL 406

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 338827709 577 HKRIHTGEKP--YKCEKCGKAFTQFSHLTVHESIHT 610
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 5.23e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 5.23e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338827709     8 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVGLTVCKPGLITCLEQRKEPWN 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 1.87e-22

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 90.22  E-value: 1.87e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 338827709    7 LLTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 7.27e-19

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.90  E-value: 7.27e-19
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 338827709   8 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-610 1.09e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 206 FDNFSNLHRRNISNTGEKPFKC--QECGKSFQMLSFLTEHQKIHT-GKKFQKCGECGKTFIQCSHFTEPENIDTGEKPYK 282
Cdd:COG5048   43 FSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHnNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 283 CQECNNVIKTCSVLTKNriyaggehyrceefgkvFNQCSHLTEhehgteekpCKYEECSSVFISCSSLSNQQMILAGEKL 362
Cdd:COG5048  123 LSSHSLPPSSRDPQLPD-----------------LLSISNLRN---------NPLPGNNSSSVNTPQSNSLHPPLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 363 SKCETWYKGFNHSPNPSkhqrneIGGKPFKCEECDSIFKWFSDLTKHKRIHTGEKPYKCDECgkayTQSSHLSEHRRIHT 442
Cdd:COG5048  177 SKDPSSNLSLLISSNVS------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN----SQLSPKSLLSQSPS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 443 GEKP-YQCEECGKVFRTCSSLSNHKRTHSEE----------KPYTCEECGNIFKQLSDLTKHKKT--HTGE--KPYKCDE 507
Cdd:COG5048  247 SLSSsDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPY 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 508 --CGKNFTQSSNLIVHKRIHTGEKPYKCEECGR-------VFMWFSDITKHKKTHTGEKPYKCD--ECGKNFTQSSNLIV 576
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfsplLNNEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSL 406

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 338827709 577 HKRIHTGEKP--YKCEKCGKAFTQFSHLTVHESIHT 610
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
573-598 6.83e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.83e-05
                          10        20
                  ....*....|....*....|....*.
gi 338827709  573 NLIVHKRIHTGEKPYKCEKCGKAFTQ 598
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 5.23e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 5.23e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338827709     8 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVGLTVCKPGLITCLEQRKEPWN 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 7-48 1.87e-22

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 90.22  E-value: 1.87e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 338827709    7 LLTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVG 48
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 7.27e-19

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.90  E-value: 7.27e-19
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 338827709   8 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFS 46
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
206-610 1.09e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 206 FDNFSNLHRRNISNTGEKPFKC--QECGKSFQMLSFLTEHQKIHT-GKKFQKCGECGKTFIQCSHFTEPENIDTGEKPYK 282
Cdd:COG5048   43 FSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHnNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 283 CQECNNVIKTCSVLTKNriyaggehyrceefgkvFNQCSHLTEhehgteekpCKYEECSSVFISCSSLSNQQMILAGEKL 362
Cdd:COG5048  123 LSSHSLPPSSRDPQLPD-----------------LLSISNLRN---------NPLPGNNSSSVNTPQSNSLHPPLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 363 SKCETWYKGFNHSPNPSkhqrneIGGKPFKCEECDSIFKWFSDLTKHKRIHTGEKPYKCDECgkayTQSSHLSEHRRIHT 442
Cdd:COG5048  177 SKDPSSNLSLLISSNVS------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN----SQLSPKSLLSQSPS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 443 GEKP-YQCEECGKVFRTCSSLSNHKRTHSEE----------KPYTCEECGNIFKQLSDLTKHKKT--HTGE--KPYKCDE 507
Cdd:COG5048  247 SLSSsDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPY 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 508 --CGKNFTQSSNLIVHKRIHTGEKPYKCEECGR-------VFMWFSDITKHKKTHTGEKPYKCD--ECGKNFTQSSNLIV 576
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfsplLNNEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSL 406

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 338827709 577 HKRIHTGEKP--YKCEKCGKAFTQFSHLTVHESIHT 610
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
373-550 1.47e-07

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.32  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 373 NHSPNPSKHQRNEIGGKPFKCEECDSIFKWFSDLTKHKR--IHTGE--KPYKCDE--CGKAYTQSSHLSEHRRIHTGEKP 446
Cdd:COG5048  272 SSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 447 YQC--EECGKVFRTCS-----SLSNHKRTHSEEKPYTCE--ECGNIFKQLSDLTKHKKTHTGEKP--YKCDECGKNFTQS 515
Cdd:COG5048  352 AKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRH 431

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 338827709 516 SNLIVHKRIHTGEKPYKCEECGRVFMWFSDITKHK 550
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
417-478 2.45e-05

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.45e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338827709 417 KPYKCDECGKAYTQSSHLSEHRRIHTGEKPYQC--EECGKVFRTCSSLSNHKRTHSEEKPYTCE 478
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS 95
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 415-498 5.08e-05

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.86  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 415 GEKPYKCD--ECGKAYTQSSHLSEHRrIHTgekpyqceECGKVFRTCSSLSNHKRTHSEEKPYTCEECGNIFKQLSDLTK 492
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHM-LHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 338827709 493 HKKTHT 498
Cdd:COG5189  417 HRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
573-598 6.83e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.83e-05
                          10        20
                  ....*....|....*....|....*.
gi 338827709  573 NLIVHKRIHTGEKPYKCEKCGKAFTQ 598
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
405-430 1.17e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.17e-04
                          10        20
                  ....*....|....*....|....*.
gi 338827709  405 DLTKHKRIHTGEKPYKCDECGKAYTQ 430
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
489-514 2.01e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 2.01e-04
                          10        20
                  ....*....|....*....|....*.
gi 338827709  489 DLTKHKKTHTGEKPYKCDECGKNFTQ 514
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-458 2.47e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.47e-04
                          10        20
                  ....*....|....*....|....*.
gi 338827709  433 HLSEHRRIHTGEKPYQCEECGKVFRT 458
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
548-570 6.78e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.78e-04
                          10        20
                  ....*....|....*....|...
gi 338827709  548 KHKKTHTGEKPYKCDECGKNFTQ 570
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
517-540 8.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.18e-04
                          10        20
                  ....*....|....*....|....
gi 338827709  517 NLIVHKRIHTGEKPYKCEECGRVF 540
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 503-525 2.95e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.95e-03
                          10        20
                  ....*....|....*....|...
gi 338827709  503 YKCDECGKNFTQSSNLIVHKRIH 525
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 559-581 2.95e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 2.95e-03
                          10        20
                  ....*....|....*....|...
gi 338827709  559 YKCDECGKNFTQSSNLIVHKRIH 581
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
501-594 3.43e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338827709 501 KPYKCDECGKNFTQSSNLIVHKRIHTGEKPYKCEECGrvfmwfsditkhkkthtgekpykcdeCGKNFTQSSNLIVHKRI 580
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSG--------------------------CDKSFSRPLELSRHLRT 85

                         90
                 ....*....|....
gi 338827709 581 HTGEKPYKCEKCGK 594
Cdd:COG5048   86 HHNNPSDLNSKSLP 99
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 447-469 4.54e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.54e-03
                          10        20
                  ....*....|....*....|...
gi 338827709  447 YQCEECGKVFRTCSSLSNHKRTH 469
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 419-441 8.34e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 8.34e-03
                          10        20
                  ....*....|....*....|...
gi 338827709  419 YKCDECGKAYTQSSHLSEHRRIH 441
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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